1do6 Summary

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CRYSTAL STRUCTURE OF SUPEROXIDE REDUCTASE IN THE OXIDIZED STATE AT 2.0 ANGSTROM RESOLUTION

The structure was published by Yeh, A.P., Hu, Y., Jenney Jr., F.E., Adams, M.W., and Rees, D.C., in 2000 in a paper entitled "Structures of the superoxide reductase from Pyrococcus furiosus in the oxidized and reduced states." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.0 Å and deposited in 1999.

The experimental data on which the structure is based was not deposited.

This PDB entry contains multiple copies of the structure of SUPEROXIDE REDUCTASE.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule most likely forms homotetramers.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A SUPEROXIDE REDUCTASE P82385 (1-124) (SOR_PYRFU)search Pyrococcus furiosus DSM 3638search 100% 124 100%
B SUPEROXIDE REDUCTASE P82385 (1-124) (SOR_PYRFU)search Pyrococcus furiosus DSM 3638search 100% 124 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P82385 (1 - 124) SUPEROXIDE REDUCTASE Pyrococcus furiosus

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B (P82385) Superoxide reductase-likesearch Immunoglobulin-likesearch PF01880: Desulfoferrodoxinsearch

Chain ID Molecular function (GO) Biological process (GO)
A, B (P82385) superoxide reductase activitysearch metal ion bindingsearch oxidoreductase activitysearch iron ion bindingsearch oxidation-reduction processsearch

Chain InterPro annotation
A, B Desulfoferrodoxin, ferrous iron-binding domainsearch